 |
PDBsum entry 5j1i
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Structural protein
|
PDB id
|
|
|
|
5j1i
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
 |
|
Title
|
 |
The structure of the plakin domain of plectin reveals an extended rod-Like shape.
|
 |
|
Authors
|
 |
E.Ortega,
J.A.Manso,
R.M.Buey,
A.M.Carballido,
A.Carabias,
A.Sonnenberg,
J.M.De pereda.
|
 |
|
Ref.
|
 |
J Biol Chem, 2016,
291,
18643-18662.
[DOI no: ]
|
 |
|
PubMed id
|
 |
|
 |
 |
|
Abstract
|
 |
|
Plakins are large multi-domain proteins that interconnect cytoskeletal
structures. Plectin is a prototypical plakin that tethers intermediate filaments
to membrane-associated complexes. Most plakins contain a plakin domain formed by
up to nine spectrin repeats (SR1-SR9) and an SH3 domain. The plakin domains of
plectin and other plakins harbor binding sites for junctional proteins. We have
combined x-ray crystallography with small angle x-ray scattering (SAXS) to
elucidate the structure of the plakin domain of plectin, extending our previous
analysis of the SR1 to SR5 region. Two crystal structures of the SR5-SR6 region
allowed us to characterize its uniquely wide inter-repeat conformational
variability. We also report the crystal structures of the SR7-SR8 region,
refined to 1.8 Å, and the SR7-SR9 at lower resolution. The SR7-SR9 region,
which is conserved in all other plakin domains, forms a rigid segment stabilized
by uniquely extensive inter-repeat contacts mediated by unusually long helices
in SR8 and SR9. Using SAXS we show that in solution the SR3-SR6 and SR7-SR9
regions are rod-like segments and that SR3-SR9 of plectin has an extended shape
with a small central kink. Other plakins, such as bullous pemphigoid antigen 1
and microtubule and actin cross-linking factor 1, are likely to have similar
extended plakin domains. In contrast, desmoplakin has a two-segment structure
with a central flexible hinge. The continuous versus segmented structures of the
plakin domains of plectin and desmoplakin give insight into how different
plakins might respond to tension and transmit mechanical signals.
|
 |
|
|
|
|
 |